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Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation

Abstract

Protein fibrillation leads to formation of amyloids—linear aggregates that are hallmarks of many serious diseases, including Alzheimer’s and Parkinson’s diseases. In this work, we investigate the fibrillation of a short peptide (K-peptide) from the amyloidogenic core of hen egg white lysozyme in the presence of dimethyl sulfoxide or urea. During the studies, a variety of spectroscopic methods were used: fluorescence spectroscopy and the Thioflavin T assay, circular dichroism, Fourier-transform infrared spectroscopy, optical density measurements, dynamic light scattering and intrinsic fluorescence. Additionally, the presence of amyloids was confirmed by atomic force microscopy. The obtained results show that the K-peptide is highly prone to form fibrillar aggregates. The measurements also confirm the weak impact of dimethyl sulfoxide on peptide fibrillation and distinct influence of urea. We believe that the K-peptide has higher amyloidogenic propensity than the whole protein, i.e., hen egg white lysozyme, most likely due to the lack of the first step of amyloidogenesis—partial unfolding of the native structure. Urea influences the second step of K-peptide amyloidogenesis, i.e., folding into amyloids.

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Details

Category:
Articles
Type:
artykuły w czasopismach
Published in:
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES no. 23,
ISSN: 1661-6596
Language:
English
Publication year:
2022
Bibliographic description:
Wawer J., Karczewski J., Aranowski R., Piątek R., Augustin-Nowacka D., Bruździak P.: Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation// INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES -Vol. 23,iss. 6 (2022), s.3027-
DOI:
Digital Object Identifier (open in new tab) 10.3390/ijms23063027
Sources of funding:
  • Free publication
Verified by:
Gdańsk University of Technology

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